ID EPHB2_HUMAN Reviewed; 1055 AA.
AC P29323; O43477; Q5T0U6; Q5T0U7; Q5T0U8;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 5.
DT 27-MAR-2024, entry version 256.
DE RecName: Full=Ephrin type-B receptor 2;
DE EC=2.7.10.1;
DE AltName: Full=Developmentally-regulated Eph-related tyrosine kinase;
DE AltName: Full=ELK-related tyrosine kinase;
DE AltName: Full=EPH tyrosine kinase 3;
DE AltName: Full=EPH-like kinase 5;
DE Short=EK5;
DE Short=hEK5;
DE AltName: Full=Renal carcinoma antigen NY-REN-47;
DE AltName: Full=Tyrosine-protein kinase TYRO5;
DE AltName: Full=Tyrosine-protein kinase receptor EPH-3;
DE Contains:
DE RecName: Full=EphB2/CTF1 {ECO:0000250|UniProtKB:P54763};
DE Contains:
DE RecName: Full=EphB2/CTF2 {ECO:0000250|UniProtKB:P54763};
DE Flags: Precursor;
GN Name=EPHB2; Synonyms=DRT, EPHT3, EPTH3, ERK, HEK5, TYRO5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=8033077;
RA Kiyokawa E., Takai S., Tanaka M., Iwase T., Suzuki M., Xiang Y.Y.,
RA Naito Y., Yamada K., Sugimura H., Kino I.;
RT "Overexpression of ERK, an EPH family receptor protein tyrosine kinase, in
RT various human tumors.";
RL Cancer Res. 54:3645-3650(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Fetal brain;
RX PubMed=8589679; DOI=10.1093/hmg/4.11.2033;
RA Ikegaki N., Tang X.X., Liu X.-G., Biegel J.A., Allen C., Yoshioka A.,
RA Sulman E.P., Brodeur G.M., Pleasure D.E.;
RT "Molecular characterization and chromosomal localization of DRT (EPHT3): a
RT developmentally regulated human protein-tyrosine kinase gene of the EPH
RT family.";
RL Hum. Mol. Genet. 4:2033-2045(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=9696046; DOI=10.1038/sj.onc.1201960;
RA Tang X.X., Pleasure D.E., Brodeur G.M., Ikegaki N.;
RT "A variant transcript encoding an isoform of the human protein tyrosine
RT kinase EPHB2 is generated by alternative splicing and alternative use of
RT polyadenylation signals.";
RL Oncogene 17:521-526(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-986 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=7898931;
RA Fox G.M., Holst P.L., Chute H.T., Lindberg R.A., Janssen A.M., Basu R.,
RA Welcher A.A.;
RT "cDNA cloning and tissue distribution of five human EPH-like receptor
RT protein-tyrosine kinases.";
RL Oncogene 10:897-905(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 509-986 (ISOFORM 2).
RC TISSUE=Fetal brain;
RX PubMed=7601466; DOI=10.1016/0888-7543(95)80224-a;
RA Saito T., Seki N., Matsuda Y., Kitahara M., Murata M., Kanda N., Nomura N.,
RA Yamamoto T., Hori T.-A.;
RT "Identification of the human ERK gene as a putative receptor tyrosine
RT kinase and its chromosomal localization to 1p36.1: a comparative mapping of
RT human, mouse, and rat chromosomes.";
RL Genomics 26:382-384(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 640-986 (ISOFORM 2).
RC TISSUE=Gastric carcinoma;
RX PubMed=7688222; DOI=10.1006/bbrc.1993.1878;
RA Iwase T., Tanaka M., Suzuki M., Naito Y., Sugimura H., Kino I.;
RT "Identification of protein-tyrosine kinase genes preferentially expressed
RT in embryo stomach and gastric cancer.";
RL Biochem. Biophys. Res. Commun. 194:698-705(1993).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 652-712.
RX PubMed=1648701;
RA Chan J., Watt V.M.;
RT "eek and erk, new members of the eph subclass of receptor protein-tyrosine
RT kinases.";
RL Oncogene 6:1057-1061(1991).
RN [9]
RP NOMENCLATURE.
RX PubMed=9267020; DOI=10.1016/s0092-8674(00)80500-0;
RG Eph nomenclature committee;
RT "Unified nomenclature for Eph family receptors and their ligands, the
RT ephrins.";
RL Cell 90:403-404(1997).
RN [10]
RP IDENTIFICATION AS A RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
RP POLYUBIQUITINATION, AND INTERACTION WITH SPSB1 AND SPSB4.
RX PubMed=28931592; DOI=10.1091/mbc.e17-07-0450;
RA Okumura F., Joo-Okumura A., Obara K., Petersen A., Nishikimi A., Fukui Y.,
RA Nakatsukasa K., Kamura T.;
RT "Ubiquitin ligase SPSB4 diminishes cell repulsive responses mediated by
RT EphB2.";
RL Mol. Biol. Cell 28:3532-3541(2017).
RN [14]
RP UBIQUITINATION BY RNF186, AND MUTAGENESIS OF LYS-787 AND LYS-891.
RX PubMed=33280498; DOI=10.1080/15548627.2020.1851496;
RA Zhang H., Cui Z., Cheng D., Du Y., Guo X., Gao R., Chen J., Sun W., He R.,
RA Ma X., Peng Q., Martin B.N., Yan W., Rong Y., Wang C.;
RT "RNF186 regulates EFNB1 (ephrin B1)-EPHB2-induced autophagy in the colonic
RT epithelial cells for the maintenance of intestinal homeostasis.";
RL Autophagy 17:3030-3047(2021).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 910-986 (ISOFORM SHORT).
RX PubMed=9933164; DOI=10.1126/science.283.5403.833;
RA Thanos C.D., Goodwill K.E., Bowie J.U.;
RT "Oligomeric structure of the human EphB2 receptor SAM domain.";
RL Science 283:833-836(1999).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 20-195 OF HOMODIMER IN COMPLEX
RP WITH ANTAGONISTIC PEPTIDE, DISULFIDE BOND, AND SUBUNIT.
RX PubMed=17897949; DOI=10.1074/jbc.m706340200;
RA Chrencik J.E., Brooun A., Recht M.I., Nicola G., Davis L.K., Abagyan R.,
RA Widmer H., Pasquale E.B., Kuhn P.;
RT "Three-dimensional structure of the EphB2 receptor in complex with an
RT antagonistic peptide reveals a novel mode of inhibition.";
RL J. Biol. Chem. 282:36505-36513(2007).
RN [17]
RP VARIANTS PROSTATE CANCER HIS-199; SER-279; ASN-679 AND MET-909, AND
RP FUNCTION AS A TUMOR SUPPRESSOR.
RX PubMed=15300251; DOI=10.1038/ng1408;
RA Huusko P., Ponciano-Jackson D., Wolf M., Kiefer J.A., Azorsa D.O.,
RA Tuzmen S., Weaver D., Robbins C., Moses T., Allinen M., Hautaniemi S.,
RA Chen Y., Elkahloun A., Basik M., Bova G.S., Bubendorf L., Lugli A.,
RA Sauter G., Schleutker J., Ozcelik H., Elowe S., Pawson T., Trent J.M.,
RA Carpten J.D., Kallioniemi O.-P., Mousses S.;
RT "Nonsense-mediated decay microarray analysis identifies mutations of EPHB2
RT in human prostate cancer.";
RL Nat. Genet. 36:979-983(2004).
RN [18]
RP VARIANTS PROSTATE CANCER SER-279; ALA-650 AND VAL-883.
RX PubMed=16155194; DOI=10.1136/jmg.2005.035790;
RA Kittles R.A., Baffoe-Bonnie A.B., Moses T.Y., Robbins C.M., Ahaghotu C.,
RA Huusko P., Pettaway C., Vijayakumar S., Bennett J., Hoke G., Mason T.,
RA Weinrich S., Trent J.M., Collins F.S., Mousses S., Bailey-Wilson J.,
RA Furbert-Harris P., Dunston G., Powell I.J., Carpten J.D.;
RT "A common nonsense mutation in EphB2 is associated with prostate cancer
RT risk in African American men with a positive family history.";
RL J. Med. Genet. 43:507-511(2006).
RN [19]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-279; GLY-289; VAL-361; ASN-678 AND
RP TRP-844.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [20]
RP VARIANT BDPLT22 CYS-745, INVOLVEMENT IN BDPLT22, AND FUNCTION.
RX PubMed=30213874; DOI=10.1182/blood-2018-04-845644;
RA Berrou E., Soukaseum C., Favier R., Adam F., Elaib Z., Kauskot A.,
RA Bordet J.C., Ballerini P., Loyau S., Feng M., Dias K., Muheidli A.,
RA Girault S., Nurden A.T., Turro E., Ouwehand W.H., Denis C.V.,
RA Jandrot-Perrus M., Rosa J.P., Nurden P., Bryckaert M.;
RT "A mutation of the human EPHB2 gene leads to a major platelet functional
RT defect.";
RL Blood 132:2067-2077(2018).
CC -!- FUNCTION: Receptor tyrosine kinase which binds promiscuously
CC transmembrane ephrin-B family ligands residing on adjacent cells,
CC leading to contact-dependent bidirectional signaling into neighboring
CC cells. The signaling pathway downstream of the receptor is referred to
CC as forward signaling while the signaling pathway downstream of the
CC ephrin ligand is referred to as reverse signaling. Functions in axon
CC guidance during development. Involved in the guidance of commissural
CC axons, that form a major interhemispheric connection between the 2
CC temporal lobes of the cerebral cortex. Also involved in guidance of
CC contralateral inner ear efferent growth cones at the midline and of
CC retinal ganglion cell axons to the optic disk. In addition to axon
CC guidance, also regulates dendritic spines development and maturation
CC and stimulates the formation of excitatory synapses. Upon activation by
CC EFNB1, abolishes the ARHGEF15-mediated negative regulation on
CC excitatory synapse formation. Controls other aspects of development
CC including angiogenesis, palate development and in inner ear development
CC through regulation of endolymph production. Forward and reverse
CC signaling through the EFNB2/EPHB2 complex regulate movement and
CC adhesion of cells that tubularize the urethra and septate the cloaca.
CC May function as a tumor suppressor. May be involved in the regulation
CC of platelet activation and blood coagulation (PubMed:30213874).
CC {ECO:0000269|PubMed:15300251, ECO:0000269|PubMed:30213874}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Heterotetramer upon binding of the ligand (By similarity). The
CC heterotetramer is composed of an ephrin dimer and a receptor dimer
CC (PubMed:17897949). Interacts (via PDZ-binding motif) with GRIP1 and
CC PICK1 (via PDZ domain) (By similarity). Interacts with ARHGEF15;
CC mediates ARHGEF15 phosphorylation, ubiquitination and degradation by
CC the proteasome (By similarity). Interacts with AQP1; involved in
CC endolymph production in the inner ear (By similarity). Interacts with
CC SPSB1 and SPSB4 (PubMed:28931592). The phosphorylated form interacts
CC with RASA1 (via SH2 domain 1) (By similarity). Interacts with EFNA5 (By
CC similarity). Interacts with SH2D3C (By similarity).
CC {ECO:0000250|UniProtKB:P54763, ECO:0000269|PubMed:17897949,
CC ECO:0000269|PubMed:28931592}.
CC -!- INTERACTION:
CC P29323; P07333: CSF1R; NbExp=2; IntAct=EBI-1059294, EBI-2835440;
CC P29323; P54764: EPHA4; NbExp=3; IntAct=EBI-1059294, EBI-5773557;
CC P29323; Q15375: EPHA7; NbExp=2; IntAct=EBI-1059294, EBI-1383428;
CC P29323; P49790: NUP153; NbExp=2; IntAct=EBI-1059294, EBI-286779;
CC P29323-3; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-25838727, EBI-6165897;
CC P29323-3; P21964-2: COMT; NbExp=3; IntAct=EBI-25838727, EBI-10200977;
CC P29323-3; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-25838727, EBI-1055254;
CC P29323-3; O14832: PHYH; NbExp=3; IntAct=EBI-25838727, EBI-721853;
CC P29323-3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25838727, EBI-5235340;
CC P29323-3; Q13148: TARDBP; NbExp=6; IntAct=EBI-25838727, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Cell projection, axon {ECO:0000250}. Cell projection, dendrite
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=EPHB2v, Long;
CC IsoId=P29323-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P29323-2; Sequence=VSP_003016, VSP_003017;
CC Name=3;
CC IsoId=P29323-3; Sequence=VSP_015713, VSP_003016, VSP_003017;
CC -!- TISSUE SPECIFICITY: Brain, heart, lung, kidney, placenta, pancreas,
CC liver and skeletal muscle. Preferentially expressed in fetal brain.
CC -!- PTM: Autophosphorylated; ligand binding stimulates autophosphorylation
CC on tyrosine residues. {ECO:0000250|UniProtKB:P54763}.
CC -!- PTM: Polyubiquitinated; ligand binding stimulates ubiquitination
CC (PubMed:28931592). Ubiquitinated by RNF186 at Lys-891, mainly through
CC 'Lys-27'-linked polyubiquitin chains (PubMed:33280498).
CC {ECO:0000269|PubMed:28931592, ECO:0000269|PubMed:33280498}.
CC -!- PTM: Ligand binding induces cleavage by matrix metalloproteinases
CC (MMPs) such as MMP7/MMP9, producing an EphB2/N-terminal fragment (NTF)
CC and a C-terminal long fragment (EphB2-LF). EphB2-LF is further cleaved
CC by MMPs, producing EphB2/CTF1 which is further cleaved by the
CC PS1/gamma-secretase producing EphB2/CTF2.
CC {ECO:0000250|UniProtKB:P54763}.
CC -!- DISEASE: Prostate cancer (PC) [MIM:176807]: A malignancy originating in
CC tissues of the prostate. Most prostate cancers are adenocarcinomas that
CC develop in the acini of the prostatic ducts. Other rare histopathologic
CC types of prostate cancer that occur in approximately 5% of patients
CC include small cell carcinoma, mucinous carcinoma, prostatic ductal
CC carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal
CC cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell
CC carcinoma and neuroendocrine carcinoma. {ECO:0000269|PubMed:15300251,
CC ECO:0000269|PubMed:16155194}. Note=The gene represented in this entry
CC may be involved in disease pathogenesis. EPHB2 mutations have been
CC found in a prostate cancer cell line derived from a brain metastasis.
CC -!- DISEASE: Bleeding disorder, platelet-type, 22 (BDPLT22) [MIM:618462]:
CC An autosomal recessive disorder characterized by increased bleeding
CC tendency due to platelet dysfunction. Clinical features include
CC epistaxis, hematomas, bleeding after minor injuries, and menorrhagia.
CC {ECO:0000269|PubMed:30213874}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; D31661; BAA06506.1; -; mRNA.
DR EMBL; L41939; AAA99310.1; -; mRNA.
DR EMBL; AF025304; AAB94602.1; -; mRNA.
DR EMBL; AL035704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L36643; AAA74244.1; -; mRNA.
DR EMBL; D37827; BAA07073.1; -; mRNA.
DR EMBL; D14717; BAA03537.1; -; mRNA.
DR EMBL; X59292; CAA41981.1; -; Genomic_DNA.
DR CCDS; CCDS229.2; -. [P29323-2]
DR CCDS; CCDS230.1; -. [P29323-3]
DR CCDS; CCDS81279.1; -. [P29323-1]
DR PIR; A57174; A57174.
DR PIR; I78842; I78842.
DR RefSeq; NP_001296122.1; NM_001309193.1. [P29323-1]
DR RefSeq; NP_004433.2; NM_004442.7. [P29323-3]
DR RefSeq; NP_059145.2; NM_017449.4. [P29323-2]
DR PDB; 1B4F; X-ray; 1.95 A; A/B/C/D/E/F/G/H=908-985.
DR PDB; 1F0M; X-ray; 2.20 A; A=908-985.
DR PDB; 2QBX; X-ray; 2.30 A; A/B=20-196.
DR PDB; 3ZFM; X-ray; 2.27 A; A=604-898.
DR PDB; 8EBL; X-ray; 1.37 A; C/D=1042-1055.
DR PDBsum; 1B4F; -.
DR PDBsum; 1F0M; -.
DR PDBsum; 2QBX; -.
DR PDBsum; 3ZFM; -.
DR PDBsum; 8EBL; -.
DR AlphaFoldDB; P29323; -.
DR BMRB; P29323; -.
DR SMR; P29323; -.
DR BioGRID; 108362; 209.
DR DIP; DIP-1162N; -.
DR IntAct; P29323; 141.
DR MINT; P29323; -.
DR STRING; 9606.ENSP00000383053; -.
DR BindingDB; P29323; -.
DR ChEMBL; CHEMBL3290; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB12843; Oleandrin.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR DrugCentral; P29323; -.
DR GuidetoPHARMACOLOGY; 1831; -.
DR GlyCosmos; P29323; 4 sites, No reported glycans.
DR GlyGen; P29323; 5 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P29323; -.
DR PhosphoSitePlus; P29323; -.
DR SwissPalm; P29323; -.
DR BioMuta; EPHB2; -.
DR DMDM; 76803654; -.
DR CPTAC; CPTAC-2786; -.
DR CPTAC; CPTAC-3205; -.
DR EPD; P29323; -.
DR jPOST; P29323; -.
DR MassIVE; P29323; -.
DR MaxQB; P29323; -.
DR PaxDb; 9606-ENSP00000363763; -.
DR PeptideAtlas; P29323; -.
DR ProteomicsDB; 54540; -. [P29323-1]
DR ProteomicsDB; 54541; -. [P29323-2]
DR ProteomicsDB; 54542; -. [P29323-3]
DR Pumba; P29323; -.
DR Antibodypedia; 30106; 748 antibodies from 41 providers.
DR DNASU; 2048; -.
DR Ensembl; ENST00000374630.8; ENSP00000363761.3; ENSG00000133216.17. [P29323-2]
DR Ensembl; ENST00000374632.7; ENSP00000363763.3; ENSG00000133216.17. [P29323-3]
DR Ensembl; ENST00000400191.7; ENSP00000383053.3; ENSG00000133216.17. [P29323-1]
DR GeneID; 2048; -.
DR KEGG; hsa:2048; -.
DR MANE-Select; ENST00000374630.8; ENSP00000363761.3; NM_017449.5; NP_059145.2. [P29323-2]
DR UCSC; uc001bge.4; human. [P29323-1]
DR AGR; HGNC:3393; -.
DR CTD; 2048; -.
DR DisGeNET; 2048; -.
DR GeneCards; EPHB2; -.
DR HGNC; HGNC:3393; EPHB2.
DR HPA; ENSG00000133216; Tissue enhanced (intestine).
DR MalaCards; EPHB2; -.
DR MIM; 176807; phenotype.
DR MIM; 600997; gene.
DR MIM; 603688; phenotype.
DR MIM; 618462; phenotype.
DR neXtProt; NX_P29323; -.
DR OpenTargets; ENSG00000133216; -.
DR Orphanet; 1331; Familial prostate cancer.
DR PharmGKB; PA27825; -.
DR VEuPathDB; HostDB:ENSG00000133216; -.
DR eggNOG; KOG0196; Eukaryota.
DR GeneTree; ENSGT00940000155503; -.
DR InParanoid; P29323; -.
DR OMA; GAINCIC; -.
DR OrthoDB; 1614410at2759; -.
DR PhylomeDB; P29323; -.
DR TreeFam; TF315608; -.
DR BRENDA; 2.7.10.1; 2681.
DR PathwayCommons; P29323; -.
DR Reactome; R-HSA-2682334; EPH-Ephrin signaling.
DR Reactome; R-HSA-373760; L1CAM interactions.
DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
DR Reactome; R-HSA-3928664; Ephrin signaling.
DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR SignaLink; P29323; -.
DR SIGNOR; P29323; -.
DR BioGRID-ORCS; 2048; 11 hits in 1193 CRISPR screens.
DR ChiTaRS; EPHB2; human.
DR EvolutionaryTrace; P29323; -.
DR GeneWiki; EPH_receptor_B2; -.
DR GenomeRNAi; 2048; -.
DR Pharos; P29323; Tchem.
DR PRO; PR:P29323; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P29323; Protein.
DR Bgee; ENSG00000133216; Expressed in ganglionic eminence and 165 other cell types or tissues.
DR ExpressionAtlas; P29323; baseline and differential.
DR Genevisible; P29323; HS.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0098794; C:postsynapse; TAS:ARUK-UCL.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
DR GO; GO:0001540; F:amyloid-beta binding; ISS:ARUK-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008046; F:axon guidance receptor activity; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:ARUK-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0007413; P:axonal fasciculation; ISS:UniProtKB.
DR GO; GO:0042113; P:B cell activation; IMP:ARUK-UCL.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IEA:Ensembl.
DR GO; GO:0071679; P:commissural neuron axon guidance; ISS:UniProtKB.
DR GO; GO:0022038; P:corpus callosum development; ISS:UniProtKB.
DR GO; GO:0060996; P:dendritic spine development; ISS:UniProtKB.
DR GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0021934; P:hindbrain tangential cell migration; IEA:Ensembl.
DR GO; GO:0042472; P:inner ear morphogenesis; ISS:UniProtKB.
DR GO; GO:0007612; P:learning; ISS:ARUK-UCL.
DR GO; GO:0007611; P:learning or memory; ISS:ARUK-UCL.
DR GO; GO:0050771; P:negative regulation of axonogenesis; IEA:Ensembl.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IMP:ARUK-UCL.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:ARUK-UCL.
DR GO; GO:1904782; P:negative regulation of NMDA glutamate receptor activity; ISS:ARUK-UCL.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:ARUK-UCL.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:ARUK-UCL.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; ISS:ARUK-UCL.
DR GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
DR GO; GO:0106028; P:neuron projection retraction; IEA:Ensembl.
DR GO; GO:0021631; P:optic nerve morphogenesis; IEA:Ensembl.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:ARUK-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IGI:ARUK-UCL.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:ARUK-UCL.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IMP:ARUK-UCL.
DR GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISS:ARUK-UCL.
DR GO; GO:1904783; P:positive regulation of NMDA glutamate receptor activity; ISS:ARUK-UCL.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; IEA:Ensembl.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0031915; P:positive regulation of synaptic plasticity; ISS:ARUK-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:ARUK-UCL.
DR GO; GO:0097104; P:postsynaptic membrane assembly; IEA:Ensembl.
DR GO; GO:2000785; P:regulation of autophagosome assembly; IDA:UniProt.
DR GO; GO:2000822; P:regulation of behavioral fear response; IEA:Ensembl.
DR GO; GO:0030193; P:regulation of blood coagulation; IMP:UniProtKB.
DR GO; GO:0050878; P:regulation of body fluid levels; ISS:UniProtKB.
DR GO; GO:0051489; P:regulation of filopodium assembly; IEA:Ensembl.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISS:ARUK-UCL.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR GO; GO:2000316; P:regulation of T-helper 17 type immune response; IEA:Ensembl.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl.
DR GO; GO:0060021; P:roof of mouth development; ISS:UniProtKB.
DR GO; GO:0120192; P:tight junction assembly; IEA:Ensembl.
DR GO; GO:0099557; P:trans-synaptic signaling by trans-synaptic complex, modulating synaptic transmission; IEA:Ensembl.
DR GO; GO:0001655; P:urogenital system development; ISS:UniProtKB.
DR GO; GO:0110077; P:vesicle-mediated intercellular transport; IEA:Ensembl.
DR CDD; cd10477; EphR_LBD_B2; 1.
DR CDD; cd00063; FN3; 2.
DR CDD; cd05065; PTKc_EphR_B; 1.
DR CDD; cd09552; SAM_EPH-B2; 1.
DR CDD; cd00185; TNFRSF; 1.
DR Gene3D; 2.60.40.1770; ephrin a2 ectodomain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR034238; EphB2_rcpt_lig-bd.
DR InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR PANTHER; PTHR46877:SF11; EPHRIN TYPE-B RECEPTOR 2; 1.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF01404; Ephrin_lbd; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR PRINTS; PR00014; FNTYPEIII.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00615; EPH_lbd; 1.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS51550; EPH_LBD; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane;
KW Cell projection; Developmental protein; Disease variant; Disulfide bond;
KW Glycoprotein; Isopeptide bond; Kinase; Membrane; Neurogenesis;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Signal; Transferase; Transmembrane; Transmembrane helix; Tumor suppressor;
KW Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1055
FT /note="Ephrin type-B receptor 2"
FT /id="PRO_0000016827"
FT CHAIN 536..986
FT /note="EphB2/CTF1"
FT /evidence="ECO:0000250|UniProtKB:P54763"
FT /id="PRO_0000445961"
FT CHAIN 562..986
FT /note="EphB2/CTF2"
FT /evidence="ECO:0000250|UniProtKB:P54763"
FT /id="PRO_0000445962"
FT TOPO_DOM 19..543
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..1055
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 20..202
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 324..434
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 435..530
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 621..884
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 913..977
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 990..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 984..986
FT /note="PDZ-binding (in isoform 2)"
FT /evidence="ECO:0000255"
FT COMPBIAS 999..1049
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 746
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 627..635
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 653
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 535..536
FT /note="Cleavage; by a metalloproteinase"
FT /evidence="ECO:0000250|UniProtKB:P54763"
FT SITE 561..562
FT /note="Cleavage; by gamma-secretase/PS1"
FT /evidence="ECO:0000250|UniProtKB:P54763"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..184
FT /evidence="ECO:0000269|PubMed:17897949"
FT DISULFID 97..107
FT /evidence="ECO:0000269|PubMed:17897949"
FT CROSSLNK 891
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:33280498"
FT VAR_SEQ 568
FT /note="R -> RR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:8589679"
FT /id="VSP_015713"
FT VAR_SEQ 986
FT /note="G -> V (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:7601466,
FT ECO:0000303|PubMed:7688222, ECO:0000303|PubMed:7898931,
FT ECO:0000303|PubMed:8033077, ECO:0000303|PubMed:8589679"
FT /id="VSP_003016"
FT VAR_SEQ 987..1055
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:7601466,
FT ECO:0000303|PubMed:7688222, ECO:0000303|PubMed:7898931,
FT ECO:0000303|PubMed:8033077, ECO:0000303|PubMed:8589679"
FT /id="VSP_003017"
FT VARIANT 199
FT /note="R -> H (in prostate cancer; dbSNP:rs201754821)"
FT /evidence="ECO:0000269|PubMed:15300251"
FT /id="VAR_032853"
FT VARIANT 279
FT /note="A -> S (in prostate cancer; dbSNP:rs35882952)"
FT /evidence="ECO:0000269|PubMed:15300251,
FT ECO:0000269|PubMed:16155194, ECO:0000269|PubMed:17344846"
FT /id="VAR_032854"
FT VARIANT 289
FT /note="C -> G"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042172"
FT VARIANT 361
FT /note="I -> V (in dbSNP:rs56180036)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042173"
FT VARIANT 650
FT /note="V -> A (in prostate cancer; dbSNP:rs142173175)"
FT /evidence="ECO:0000269|PubMed:16155194"
FT /id="VAR_032855"
FT VARIANT 678
FT /note="D -> N (in dbSNP:rs28936395)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042174"
FT VARIANT 679
FT /note="H -> N (in prostate cancer)"
FT /evidence="ECO:0000269|PubMed:15300251"
FT /id="VAR_032856"
FT VARIANT 745
FT /note="R -> C (in BDPLT22; dbSNP:rs761749948)"
FT /evidence="ECO:0000269|PubMed:30213874"
FT /id="VAR_082702"
FT VARIANT 844
FT /note="R -> W (in dbSNP:rs55826626)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042175"
FT VARIANT 883
FT /note="M -> V (in prostate cancer; dbSNP:rs372653137)"
FT /evidence="ECO:0000269|PubMed:16155194"
FT /id="VAR_032857"
FT VARIANT 909
FT /note="I -> M (in prostate cancer)"
FT /evidence="ECO:0000269|PubMed:15300251"
FT /id="VAR_032858"
FT MUTAGEN 787
FT /note="K->R: No loss of ubiquitination by RNF186."
FT /evidence="ECO:0000269|PubMed:33280498"
FT MUTAGEN 891
FT /note="K->R: Complete loss of ubiquitination by RNF186."
FT /evidence="ECO:0000269|PubMed:33280498"
FT CONFLICT 1..20
FT /note="MALRRLGAALLLLPLLAAVE -> MWVPVLALPVCTYA (in Ref. 1;
FT BAA06506)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="G -> D (in Ref. 1; BAA06506)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="K -> KQ (in Ref. 1; BAA06506)"
FT /evidence="ECO:0000305"
FT CONFLICT 495..496
FT /note="Missing (in Ref. 5; AAA74244)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="E -> D (in Ref. 1; BAA06506)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="M -> I (in Ref. 5; AAA74244)"
FT /evidence="ECO:0000305"
FT CONFLICT 671
FT /note="A -> R (in Ref. 7; BAA03537)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="I -> F (in Ref. 5; AAA74244)"
FT /evidence="ECO:0000305"
FT CONFLICT 853
FT /note="S -> A (in Ref. 1; BAA06506, 6; BAA07073 and 7;
FT BAA03537)"
FT /evidence="ECO:0000305"
FT CONFLICT 923
FT /note="E -> K (in Ref. 1; BAA06506, 6; BAA07073 and 7;
FT BAA03537)"
FT /evidence="ECO:0000305"
FT CONFLICT 958
FT /note="V -> L (in Ref. 2; AAA99310)"
FT /evidence="ECO:0000305"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:2QBX"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:2QBX"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:2QBX"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:2QBX"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:2QBX"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2QBX"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2QBX"
FT STRAND 84..94
FT /evidence="ECO:0007829|PDB:2QBX"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2QBX"
FT STRAND 111..120
FT /evidence="ECO:0007829|PDB:2QBX"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:2QBX"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:2QBX"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:2QBX"
FT STRAND 155..166
FT /evidence="ECO:0007829|PDB:2QBX"
FT STRAND 171..183
FT /evidence="ECO:0007829|PDB:2QBX"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:2QBX"
FT HELIX 618..620
FT /evidence="ECO:0007829|PDB:3ZFM"
FT STRAND 621..626
FT /evidence="ECO:0007829|PDB:3ZFM"
FT STRAND 635..640
FT /evidence="ECO:0007829|PDB:3ZFM"
FT STRAND 648..655
FT /evidence="ECO:0007829|PDB:3ZFM"
FT HELIX 661..674
FT /evidence="ECO:0007829|PDB:3ZFM"
FT STRAND 685..689
FT /evidence="ECO:0007829|PDB:3ZFM"
FT STRAND 691..700
FT /evidence="ECO:0007829|PDB:3ZFM"
FT HELIX 707..712
FT /evidence="ECO:0007829|PDB:3ZFM"
FT TURN 713..716
FT /evidence="ECO:0007829|PDB:3ZFM"
FT HELIX 720..739
FT /evidence="ECO:0007829|PDB:3ZFM"
FT HELIX 749..751
FT /evidence="ECO:0007829|PDB:3ZFM"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:3ZFM"
FT STRAND 760..762
FT /evidence="ECO:0007829|PDB:3ZFM"
FT HELIX 790..792
FT /evidence="ECO:0007829|PDB:3ZFM"
FT HELIX 795..800
FT /evidence="ECO:0007829|PDB:3ZFM"
FT HELIX 805..820
FT /evidence="ECO:0007829|PDB:3ZFM"
FT TURN 826..829
FT /evidence="ECO:0007829|PDB:3ZFM"
FT HELIX 832..840
FT /evidence="ECO:0007829|PDB:3ZFM"
FT HELIX 853..862
FT /evidence="ECO:0007829|PDB:3ZFM"
FT HELIX 873..885
FT /evidence="ECO:0007829|PDB:3ZFM"
FT HELIX 887..890
FT /evidence="ECO:0007829|PDB:3ZFM"
FT HELIX 918..924
FT /evidence="ECO:0007829|PDB:1B4F"
FT HELIX 928..930
FT /evidence="ECO:0007829|PDB:1B4F"
FT HELIX 931..936
FT /evidence="ECO:0007829|PDB:1B4F"
FT HELIX 942..945
FT /evidence="ECO:0007829|PDB:1B4F"
FT HELIX 950..955
FT /evidence="ECO:0007829|PDB:1B4F"
FT HELIX 961..982
FT /evidence="ECO:0007829|PDB:1B4F"
FT HELIX 1050..1052
FT /evidence="ECO:0007829|PDB:8EBL"
FT MOD_RES P29323-2:983
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES P29323-3:984
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
SQ SEQUENCE 1055 AA; 117493 MW; 4F8BFEDC45986483 CRC64;
MALRRLGAAL LLLPLLAAVE ETLMDSTTAT AELGWMVHPP SGWEEVSGYD ENMNTIRTYQ
VCNVFESSQN NWLRTKFIRR RGAHRIHVEM KFSVRDCSSI PSVPGSCKET FNLYYYEADF
DSATKTFPNW MENPWVKVDT IAADESFSQV DLGGRVMKIN TEVRSFGPVS RSGFYLAFQD
YGGCMSLIAV RVFYRKCPRI IQNGAIFQET LSGAESTSLV AARGSCIANA EEVDVPIKLY
CNGDGEWLVP IGRCMCKAGF EAVENGTVCR GCPSGTFKAN QGDEACTHCP INSRTTSEGA
TNCVCRNGYY RADLDPLDMP CTTIPSAPQA VISSVNETSL MLEWTPPRDS GGREDLVYNI
ICKSCGSGRG ACTRCGDNVQ YAPRQLGLTE PRIYISDLLA HTQYTFEIQA VNGVTDQSPF
SPQFASVNIT TNQAAPSAVS IMHQVSRTVD SITLSWSQPD QPNGVILDYE LQYYEKELSE
YNATAIKSPT NTVTVQGLKA GAIYVFQVRA RTVAGYGRYS GKMYFQTMTE AEYQTSIQEK
LPLIIGSSAA GLVFLIAVVV IAIVCNRRGF ERADSEYTDK LQHYTSGHMT PGMKIYIDPF
TYEDPNEAVR EFAKEIDISC VKIEQVIGAG EFGEVCSGHL KLPGKREIFV AIKTLKSGYT
EKQRRDFLSE ASIMGQFDHP NVIHLEGVVT KSTPVMIITE FMENGSLDSF LRQNDGQFTV
IQLVGMLRGI AAGMKYLADM NYVHRDLAAR NILVNSNLVC KVSDFGLSRF LEDDTSDPTY
TSALGGKIPI RWTAPEAIQY RKFTSASDVW SYGIVMWEVM SYGERPYWDM TNQDVINAIE
QDYRLPPPMD CPSALHQLML DCWQKDRNHR PKFGQIVNTL DKMIRNPNSL KAMAPLSSGI
NLPLLDRTIP DYTSFNTVDE WLEAIKMGQY KESFANAGFT SFDVVSQMMM EDILRVGVTL
AGHQKKILNS IQVMRAQMNQ IQSVEGQPLA RRPRATGRTK RCQPRDVTKK TCNSNDGKKK
GMGKKKTDPG RGREIQGIFF KEDSHKESND CSCGG
//
